Structural determinants for transport of lactase phlorizin-hydrolase in the early secretory pathway as a multi-domain membrane glycoprotein

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• 作者：Lena Diekmann^a ; ¹ ; Marc Behrendt^b ; ¹ ; Mahdi Amiri^a ; Hassan Y. Naim^a ; ^{Hassan.Naim@tiho-hannover.de}
• 关键词：PNGase F ; Peptide -N-Glycosidase F ; endo H ; endoglycosidase H ; ER ; endoplasmic reticulum ; LPH ; lactase-phlorizin hydrolase (all forms) ; LPHh ; mannose-rich precursor ; LPHc ; complex glycosylated precursor ; TGN ; trans-Golgi network
• 刊名：Biochimica et Biophysica Acta (BBA) - General Subjects
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：1861
• 期：1
• 页码：3119-3128
• 全文大小：1510 K
• 卷排序：1861

文摘

LPH trafficking analyzed by directed restructuring of the domain compositions. A stretch in domain II of LPH retains partially folded protein in the ER. Domain I can restore trafficking of chimeras that retained via domain II. Dimerization has a role in function and life cycle of LPH but not in its ER exit. This study presents an example for analyzing other multi-domain proteins.